Author

L. Gremer

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Organism:human· 2 Assay:cryo-EM· 1 Research Focus:differential expression· 1 Approach:genetic perturbation / CRISPR· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

D. Willbold· 4 shared T. Kupreichyk· 2 shared W. Hoyer· 2 shared A. Mirzaiebadizi· 1 shared A. Szczepaniak· 1 shared A. V. Busley· 1 shared B. Gault· 1 shared B. Wollnik· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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4 shared papersBiochemistry

D. Willbold

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

LZTR1 polymerization provokes cardiac pathology in recessive Noonan syndrome

A. V. Busley, O. Gutierrez-Gutierrez, E. Hammer, F. Koitka, A. Mirzaiebadizi, M. Steinegger, C. Pape, L. Boehmer, H. Schroeder, M. Kleinsorge, M. Engler, I. C. Cirstea, L. Gremer, D. Willbold, J. Altmueller, , L. Cyganek

This study identifies a novel LZTR1 variant causing cardiac hypertrophy by altering protein polymerization and ubiquitin ligase function, showing genetic correction can rescue the phenotype.

bioRxiv · Jan 10, 2023Cell Biology

Structural Basis for the Inhibition of IAPP Fibril Formation by the Hsp60 Co-Chaperonin Prefoldin

R. Toerner, T. Kupreichyk, L. Gremer, E. Colas Debled, D. Fenel, P. Gans, D. Willbold, G. Schoehn, W. Hoyer, J. Boisbouvier

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

bioRxiv · Oct 20, 2021Biophysics

Amyloid fibril structure of islet amyloid polypeptide by cryo-electron microscopy reveals similarities with amyloid beta

C. Roeder, T. Kupreichyk, L. Gremer, L. U. Schaefer, K. R. Pothula, R. B. Ravelli, D. Willbold, W. Hoyer, G. F. Schroeder

This study uses cryo-EM to reveal the structure of IAPP fibrils, showing similarities with Aβ polymorphs and linking genetic mutations to amyloid formation.

bioRxiv · Feb 11, 2020Biochemistry

An atomic-scale view at the composition ofamyloid-beta fibrils by atom probe tomography

K. A. K. Rusitzka, L. T. Stephenson, A. Szczepaniak, L. Gremer, D. Raabe, D. Willbold, B. Gault

The paper uses atom probe tomography to analyze the composition of amyloid-beta fibrils at the atomic scale, revealing structural and chemical details.

bioRxiv · Jun 20, 2018Biochemistry